3MO8
PWWP Domain of Human Bromodomain and PHD finger-containing protein 1 In Complex with Trimethylated H3K36 Peptide
Summary for 3MO8
Entry DOI | 10.2210/pdb3mo8/pdb |
Related | 3L42 |
Descriptor | Peregrin, Histone H3.2 TRIMETHYLATED H3K36 PEPTIDE (3 entities in total) |
Functional Keywords | peregrin, protein br140, histone h3 acetylation, transcription, structural genomics consortium, sgc |
Biological source | Homo sapiens (human) More |
Cellular location | Nucleus : P55201 Q71DI3 |
Total number of polymer chains | 2 |
Total formula weight | 16433.07 |
Authors | Lam, R.,Zeng, H.,Ni, S.,Bountra, C.,Weigelt, J.,Arrowsmith, C.H.,Edwards, A.M.,Bochkarev, A.,Min, J.,Wu, H.,Structural Genomics Consortium (SGC) (deposition date: 2010-04-22, release date: 2010-06-02, Last modification date: 2023-09-06) |
Primary citation | Wu, H.,Zeng, H.,Lam, R.,Tempel, W.,Amaya, M.F.,Xu, C.,Dombrovski, L.,Qiu, W.,Wang, Y.,Min, J. Structural and Histone Binding Ability Characterizations of Human PWWP Domains. Plos One, 6:e18919-e18919, 2011 Cited by PubMed Abstract: The PWWP domain was first identified as a structural motif of 100-130 amino acids in the WHSC1 protein and predicted to be a protein-protein interaction domain. It belongs to the Tudor domain 'Royal Family', which consists of Tudor, chromodomain, MBT and PWWP domains. While Tudor, chromodomain and MBT domains have long been known to bind methylated histones, PWWP was shown to exhibit histone binding ability only until recently. PubMed: 21720545DOI: 10.1371/journal.pone.0018919 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.69 Å) |
Structure validation
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